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Literature summary extracted from

  • Grant, G.A.
    D-3-Phosphoglycerate dehydrogenase (2018), Front. Mol. Biosci., 5, 110 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.95 3-phosphooxypyruvate significant substrate inhibition Homo sapiens
1.1.1.95 3-phosphooxypyruvate significant substrate inhibition. NADH bound at or near the ASB site and reduces the amount of substrate inhibition due to substrate interaction at the ASB site Mycobacterium tuberculosis
1.1.1.95 L-serine potent inhibitor Escherichia coli
1.1.1.95 additional information CBR5884, a potent inhibitor of the human enzyme (PGDH), does not inhibit the enzyme from Mycobacterium tuberculosis Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.95 0.0032
-
3-phosphooxypyruvate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 0.015
-
3-phosphooxypyruvate pH 7.0, temperature not specified in the publication Rattus norvegicus
1.1.1.95 0.025
-
NADH pH 7.0, temperature not specified in the publication Rattus norvegicus
1.1.1.95 0.027
-
NAD+ pH 7.0, temperature not specified in the publication Rattus norvegicus
1.1.1.95 0.088
-
2-oxoglutarate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 0.17
-
3-phosphooxypyruvate pH and temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 0.4
-
D-2-hydroxyglutarate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 0.54
-
3-phospho-D-glycerate pH and temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 1.2
-
3-phospho-D-glycerate pH and temperature not specified in the publication Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.95 3-phospho-D-glycerate + NAD+ Homo sapiens
-
3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+ Mycobacterium tuberculosis enzyme in the L-serine biosynthetic pathway 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+ Escherichia coli enzyme in the L-serine biosynthetic pathway 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+ Rattus norvegicus enzyme in the L-serine biosynthetic pathway 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+ Mycobacterium tuberculosis ATCC 25618 enzyme in the L-serine biosynthetic pathway 3-phosphooxypyruvate + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.95 Escherichia coli C3SVM7
-
-
1.1.1.95 Homo sapiens O43175
-
-
1.1.1.95 Mycobacterium tuberculosis P9WNX3
-
-
1.1.1.95 Mycobacterium tuberculosis ATCC 25618 P9WNX3
-
-
1.1.1.95 Rattus norvegicus O08651
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.95 2-oxoglutarate + NADH + H+
-
Escherichia coli D-2-hydroxyglutarate + NAD+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Homo sapiens 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Homo sapiens 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Mycobacterium tuberculosis 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Escherichia coli 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Rattus norvegicus 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ enzyme in the L-serine biosynthetic pathway Mycobacterium tuberculosis 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+ enzyme in the L-serine biosynthetic pathway Escherichia coli 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+ enzyme in the L-serine biosynthetic pathway Rattus norvegicus 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phospho-D-glycerate + NAD+
-
Mycobacterium tuberculosis ATCC 25618 3-phosphooxypyruvate + NADH + H+
-
r
1.1.1.95 3-phospho-D-glycerate + NAD+ enzyme in the L-serine biosynthetic pathway Mycobacterium tuberculosis ATCC 25618 3-phosphooxypyruvate + NADH + H+
-
?
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Homo sapiens 3-phospho-D-glycerate + NAD+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Mycobacterium tuberculosis 3-phospho-D-glycerate + NAD+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Escherichia coli 3-phospho-D-glycerate + NAD+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Rattus norvegicus 3-phospho-D-glycerate + NAD+
-
r
1.1.1.95 3-phosphooxypyruvate + NADH + H+
-
Mycobacterium tuberculosis ATCC 25618 3-phospho-D-glycerate + NAD+
-
r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.95 D-3-phosphoglycerate dehydrogenase
-
Homo sapiens
1.1.1.95 D-3-phosphoglycerate dehydrogenase
-
Mycobacterium tuberculosis
1.1.1.95 D-3-phosphoglycerate dehydrogenase
-
Escherichia coli
1.1.1.95 D-3-phosphoglycerate dehydrogenase
-
Rattus norvegicus
1.1.1.95 PGDH
-
Homo sapiens
1.1.1.95 PGDH
-
Mycobacterium tuberculosis
1.1.1.95 PGDH
-
Escherichia coli
1.1.1.95 PGDH
-
Rattus norvegicus
1.1.1.95 Rv2996c
-
Mycobacterium tuberculosis
1.1.1.95 serA1
-
Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.95 0.6
-
3-phospho-D-glycerate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 0.7
-
D-2-hydroxyglutarate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 1.4
-
3-phospho-D-glycerate pH and temperature not specified in the publication Mycobacterium tuberculosis
1.1.1.95 2 8 3-phosphooxypyruvate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 12
-
2-oxoglutarate pH and temperature not specified in the publication, 12-33/s Escherichia coli
1.1.1.95 2400
-
3-phosphooxypyruvate pH and temperature not specified in the publication Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.95 NAD+
-
Homo sapiens
1.1.1.95 NAD+
-
Mycobacterium tuberculosis
1.1.1.95 NAD+
-
Escherichia coli
1.1.1.95 NAD+
-
Rattus norvegicus
1.1.1.95 NADH
-
Homo sapiens
1.1.1.95 NADH
-
Escherichia coli
1.1.1.95 NADH
-
Rattus norvegicus
1.1.1.95 NADH NADH can bind to the enzyme in the absence of substrate but that the binding constants were too slow to account for the catalytic reaction Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.1.1.95 drug target potential cancer therapy target Homo sapiens
1.1.1.95 malfunction PGDH deficiency results in metabolic defects of the nervous system whose systems range from microcephaly at birth, seizures, and psychomotor retardation Homo sapiens
1.1.1.95 metabolism enzyme in the L-serine biosynthetic pathway Mycobacterium tuberculosis
1.1.1.95 metabolism enzyme in the L-serine biosynthetic pathway Escherichia coli
1.1.1.95 metabolism enzyme in the L-serine biosynthetic pathway Rattus norvegicus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.95 0.5
-
3-phospho-D-glycerate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 2
-
D-2-hydroxyglutarate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 400
-
2-oxoglutarate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 9000
-
3-phosphooxypyruvate pH and temperature not specified in the publication Escherichia coli
1.1.1.95 10000
-
3-phosphooxypyruvate pH and temperature not specified in the publication Mycobacterium tuberculosis